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Database: UniProt/TrEMBL
Entry: A0A1Q2GZ94_9GAMM
LinkDB: A0A1Q2GZ94_9GAMM
Original site: A0A1Q2GZ94_9GAMM 
ID   A0A1Q2GZ94_9GAMM        Unreviewed;       541 AA.
AC   A0A1Q2GZ94;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AQQ00415.1};
GN   ORFNames=B0W48_11785 {ECO:0000313|EMBL:AQQ00415.1};
OS   Pseudoalteromonas aliena.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ00415.1, ECO:0000313|Proteomes:UP000188243};
RN   [1] {ECO:0000313|EMBL:AQQ00415.1, ECO:0000313|Proteomes:UP000188243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EH1 {ECO:0000313|EMBL:AQQ00415.1,
RC   ECO:0000313|Proteomes:UP000188243};
RA   Kim E., Heo E., Kim H., Kim D.;
RT   "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT   strain EH1 isolated from Arctic seawater.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP019628; AQQ00415.1; -; Genomic_DNA.
DR   KEGG; paln:B0W48_11785; -.
DR   KO; K01580; -.
DR   Proteomes; UP000188243; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000188243};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     337    337       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   541 AA;  59694 MW;  D8C4A5EB262FF53A CRC64;
     MDQKRCAVAS KESLKRIFTV PEAPDSTLSK IELEISSNLA GFLNENIAAI EKPLHEIEKD
     FQSAVIPEDP TFVSAYAQDI MEQLVAHSVH TAAPSFIGHM TSALPHFLLP LSKLMVGLNQ
     NLVKIETSKA FTPLERQVLG MMHHLAYGQE DSFYSKWMHS AKTSLGAFCS GGTVANITAL
     WIARNRLFKP DGDFRGIGAQ GLIAGMLHYG YKGLAVLISE RGHYSLGKSV DLLGIGRENL
     IGIKTSEDNK VDVGAMREKA LELESQGIKV MAIIGVAGTT ETGNIDPLNE MADLAEQINC
     HFHVDAAWGG ATLLSTTHRP LLKGIERADS ITIDAHKQMY VPMGAGLVLF KDPAATDAIE
     HHAEYILRKG SKDLGSHTLE GSRPGMAMLV HACLRVIGRK GYEMLIDRSI KKAHYFADLI
     KADEDFELIS EPELCLLTYR YVPKKIKQAI AEADAATRLD IFASLNRFTA SMQKRQRESG
     RSFVSRTRLT PSKYDNQPTV VFRVVLANPL TSGAILKDIL AEQKELAKTD PVFKKYLRKY
     M
//
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